title: Inhibition of lipases from Chromobacterium viscosum and Rhizopus oryzae by tetrahydrolipstatin.
abstract: Tetrahydrolipstatin is known as an inhibitor for pancreatic lipase but not for microbial lipases. In this paper we demonstrate that in the presence of water-insoluble substrates like tributyrin or olive oil, tetrahydrolipstatin inhibits the lipases of Chromobacterium viscosum and Rhizopus oryzae, although with different potency. In contrast to porcine pancreatic lipase, which forms an irreversible and covalent enzyme-inhibitor complex with tetrahydrolipstatin, the inhibition of the microbial lipases is reversible as the inhibitor can be removed from the enzyme-inhibitor complex by solvent extraction. Moreover, after inhibition of Chromobacterium viscosum lipase tetrahydrolipstatin remains chemically unchanged.
authors.affiliation: Institut für Biochemie, Universität Münster, Germany.
authors.forename: A P
authors.initials: AP
authors.lastname: Potthoff
authors.forename: L
authors.initials: L
authors.lastname: Haalck
authors.forename: F
authors.initials: F
authors.lastname: Spener
mesh_terms: D019840:2-Propanol / Q000494:pharmacology; D002855:Chromatography, Thin Layer; D002861:Chromobacterium / Q000201:enzymology*; D004655:Emulsions; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D007783:Lactones / Q000378:metabolism / Q000494:pharmacology*; D008049:Lipase / Q000037:antagonists & inhibitors*; D015394:Molecular Structure; D000069463:Olive Oil; D000077403:Orlistat; D010938:Plant Oils / Q000378:metabolism; D011485:Protein Binding; D012233:Rhizopus / Q000201:enzymology*; D014280:Triglycerides / Q000378:metabolism
chemical_list: D004655:Emulsions; D004791:Enzyme Inhibitors; D007783:Lactones; D000069463:Olive Oil; D010938:Plant Oils; D014280:Triglycerides; D000077403:Orlistat; D008049:Lipase; D019840:2-Propanol; C005830:tributyrin